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Myosin Heavy Chains

Myosin Heavy Chains are a class of motor proteins essential for muscle contraction and cellular movement.
These large polypeptide chains form the 'heavy' portion of the myosin protein complex, playing a critical role in the generation of force and motion within cells.
Myosin Heavy Chains exhibit diverse isoforms and tissue distributions, contributing to the specialized functions of different muscle types.
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Most cited protocols related to «Myosin Heavy Chains»

Zebrafish Ventricular Resection and Regeneration

Cited 40 times

Outbred Ekkwill strain (EK) or EK/AB mixed background zebrafish 6–12 months of age were used for ventricular resection surgeries as described previously4 (link). All transgenic strains were analyzed as hemizygotes; details of their construction are described in the separate Methods section. Animal density was maintained at ~4 fish/liter in all experiments. 4-hydroxytamoxifen (4-HT) (Sigma) dissolved with ethanol (5 mg/ml) was diluted in water to 0.5 mg/ml for intraperitoneal injections. 10% ethanol was used as a vehicle control. EGFP labeling quantification is described in the separate Methods section. Heat-shock experiments were performed as described previously27 (link), using double transgenic hsp70:dnfgfr1; cmlc2:nucDsRed2 or hsp70:dnfgfr1; gata4:EGFP animals. For BrdU incorporation experiments, 2.5 mg/ml BrdU (Sigma) was injected intraperitoneally once daily for 3 days prior to collection. Immunofluorescence, in situ hybridization, and Acid Fuchsin Orange G stains (detecting fibrin and collagen) were performed as described previously4 (link). Primary antibodies used in this study were: anti-Mef2 (rabbit; Santa Cruz Biotechnology), anti-Myosin heavy chain (F59, mouse; Developmental Studies Hybridoma Bank), anti-β-catenin (rabbit; Sigma), anti-zf Raldh2 (rabbit: Abmart), anti-BrdU (rat; Accurate), and anti-GFP (rabbit, used only for co-detection with BrdU; Invitrogen). Secondary antibodies (Invitrogen) used in this study were Alexa Fluor 594 goat anti-rabbit IgG (H+L) for anti-Mef2, Alexa Fluor 594 goat anti-mouse IgG (H+L) for F59, Alexa Fluor 594 goat anti-rat IgG (H+L) for anti-BrdU, and Alexa Fluor 488 goat anti-rabbit IgG (H+L) for anti-GFP. In situ hybridization and immunofluorescence images were taken using a Leica DM6000 microscope with a Retiga-EXi camera (Q-IMAGING), and confocal images were taken using a Leica SP2 or SP5 confocal microscope. Physiology methods are described in the separate Methods section.

Kikuchi K., Holdway J.E., Werdich A.A., Anderson R.M., Fang Y., Egnaczyk G.F., Evans T., MacRae C.A., Stainier D.Y, & Poss K.D. (2010). Primary contribution to zebrafish heart regeneration by gata4+ cardiomyocytes. Nature, 464(7288), 601-605.

Publication 2010

acid-fuchsin afimoxifene ALDH1A2 protein, human Alexa594 alexa fluor 488 Animals Animals, Transgenic anti-IgG Antibodies Bromodeoxyuridine Collagen CTNNB1 protein, human Ethanol Fibrin Fishes Fluorescent Antibody Technique Goat Heart Ventricle Heat-Shock Proteins 70 Heat-Shock Response Hemizygote Hybridomas Injections, Intraperitoneal In Situ Hybridization Mice, House Microscopy Microscopy, Confocal Myosin Heavy Chains Operative Surgical Procedures Orange G physiology Rabbits Staining Strains Zebrafish

Visualization of Endogenous Myosin in Drosophila Embryos

Cited 38 times

Heat fixation and staining with anti-myosin heavy chain (MHC) antibody did not preserve the normal organization of apical myosin observed in live squ-GFP26 (link), squ-mCherry (Myosin-mCherry), and GFP-zipper (GFP-MHC)27 (link) embryos. Therefore, endogenous GFP fluorescence was used to visualize myosin. squ-GFP embryos were fixed with 10% paraformaldehyde/heptane for 20 minutes, manually devitellinized, stained with Alexa-568 Phalloidin (Invitrogen) to visualize actin, and mounted in AquaPolymount (Poysciences, Inc.).

Martin A.C., Kaschube M, & Wieschaus E.F. (2008). Pulsed actin-myosin network contractions drive apical constriction. Nature, 457(7228), 495.

Publication 2008

Actins alexa 568 Antibodies, Anti-Idiotypic Embryo Fluorescence Heptane Myosin ATPase Myosin Heavy Chains paraform Phalloidine

Generating Talin and Vinculin Mutant Alleles in Drosophila

Cited 16 times

Details on the generation of new rhea (talin) and Vinculin alleles can be found in Supplemental Experimental Procedures.
For wing blister quantification, mitotic clones were generated in the wings of heterozygous flies by crossing rhea mutant males to w; P{w[+], Gal4}Vg[BE] P{w[+], UAS::FLP}; P{FRT}2A (with the white+ excised from P{FRT2Aw[hs]}) females. Embryonic phenotype quantification was performed on mutant embryos lacking both maternal and zygotic wild-type talin and/or vinculin, as they were obtained from germline clones generated in heterozygous mutant females by crossing rhea mutant females (with wild-type Vinculin or ΔVinc) to P{hs::FLP}1, y[1] w[118]; P{ovoD1-18}3L P{FRTw[hs]}2A (for genotypes with wild-type Vinculin) or ΔVinc w[-]; P{hs::FLP}38/CyO; P{ovoD1-18}3L P{FRTw[hs]}2A (for genotypes with ΔVinc) males. Heat shocks were performed two times for 1 hr and 15 min each at 37°C at L1 and L2 larval stages. TalinIBS2-mCherry [31 (link)] was kindly provided by H.J. Bellen. The myosin heavy chain mutant used was Mhc[1] [45 (link)], kindly provided by S.I. Bernstein. IBS2-GFP recruitment to muscle attachment sites was performed with UAS::IBS2-GFP [15 (link)] expressed in muscles with P{Gal4-Mef2.R}3 (Bloomington Drosophila Stock Center).

Klapholz B., Herbert S.L., Wellmann J., Johnson R., Parsons M, & Brown N.H. (2015). Alternative Mechanisms for Talin to Mediate Integrin Function. Current Biology, 25(7), 847-857.

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Publication 2015

Alleles Clone Cells Diptera Drosophila Embryo Females Genotype Germ Line Heat-Shock Response Heterozygote Larva Males Mothers Muscle Tissue Myosin Heavy Chains Phenotype Rhea Talin VCL protein, human Zygote

Conditional Cardiac-Specific Csn8 Knockout

Cited 15 times

The Csn8-floxed mouse model (Csn8^flox/+) was originally created in the 129/Sv background.31 (link) For the present study, it was converted to the C57BL6 inbred background through >10 generations of backcross. In the Csn8-floxed allele, exons 4 through 6 of the Csn8 gene are flanked by two loxP sites.31 (link) The transgenic (tg) mouse model with expression of Cre driven by the mouse α myosin heavy chain (Mhc6) promoter (αMHC-Cre⁺) was created and maintained in the C57BL6 background.14 From the cross-breeding scheme depicted in Fig. 1A, CSN8^flox/flox/αMHC-Cre⁺ mice (CR-Csn8KO) and littermate CSN8^flox/flox/αMHC-Cre^- mice (CTL) were obtained and used in this study. Notably, we did not observe any phenotypic difference between the CSN8^flox/flox/αMHC-Cre^- and the CSN8^+/+/αMHC-Cre⁺ mice within the time frame studied here.
The creation and validation of the FVB/N GFPdgn tg mice as a reverse reporter of UPS proteolytic function have been previously described.7 (link) The Bcl2 tg mice were previously described.36 (link) The breeding strategies to introduce the GFPdgn or the Bcl2 transgene into the CR-Csn8KO background were similar (Supplementary Fig. I). The care and use of animals in this study conform to institutional guidelines for the use of animals in research.
Western blot analyses, gel filtration, RNA dot blot analysis, echocardiography, terminal dUTP nick end-labeling (TUNEL) assays, and immunofluorescence and confocal microscopy were performed as we previously described.29 (link), 35 , 37 (link)

Su H., Li J., Menon S., Liu J., Kumarapeli A.R., Wei N, & Wang X. (2010). Perturbation of cullin deneddylation via conditional Csn8 ablation impairs the ubiquitin-proteasome system and causes cardiomyocyte necrosis and dilated cardiomyopathy in mice. Circulation research, 108(1), 40-50.

Publication 2010

Alleles Animals bcl-2 Gene Biological Assay deoxyuridine triphosphate Echocardiography Exons Gel Chromatography Genes Immunofluorescence Mice, Laboratory Mice, Transgenic Microscopy, Confocal Myosin Heavy Chains Northern Blotting Phenotype Proteolysis Reading Frames Transgenes Western Blot

Murine Models of Cardiac Hypertrophy

Cited 13 times

All experiments involving animals conformed to the Guide for the Care and Use of Laboratory Animals published by the US National Institutes of Health (NIH Publication 8^th edition, update 2011) and were approved by the Institutional Animal Care and Use Committee of the University of Texas Southwestern Medical Center. The studies were in compliance with all ethical regulations. C57BL/6N mice were used for wild-type (WT) studies. Tetracycline responsive elements (TRE)-Xbp1s mice were crossed with mice harbouring tetracycline transactivator (tTA) transcription factor driven by α-myosin heavy chain promoter (αMHC-tTA) to generate mice with cardiomyocyte-specific inducible overexpression of Xbp1s (Xbp1s TG) as previously described^{10 (link)}. iNOS knockout mice (Nos2^−/−, B6.129P2-Nos2tm1Lau/J) were purchased from Jackson Laboratory (Bar Harbor, Maine) to establish an in-house colony. ZSF1-obese (ZSF1-LeprfaLeprcp/Crl, strain code 378) and Wistar-Kyoto (WKY) rats were obtained from Charles River Laboratories (Wilmington, Massachusetts). Male adult (8/12 week-old) mice were used in the experiments. Analyses in rats were carried out when the animals reached 20 weeks of age. Mice and rats were maintained on a 12-hour light/dark cycle from 6 AM to 6 PM and had unrestricted access to food (#2916, Teklad for CHOW groups and D12492, Research Diet Inc. for the HFD groups) and water. N^[w]-nitro-l-arginine methyl ester (L-NAME; 0.5 g/L, Sigma Aldrich) was supplied in the drinking water for the indicated periods of time, after adjusting the pH to 7.4. L-N6-(1-iminoethyl)lysine (L-NIL, Cayman Chemical) was administered intraperitoneally (i.p.) at a dose of 80 mg/kg body weight twice a day for three days. Transverse aortic constriction (TAC or severe TAC, sTAC) was surgically induced as previously described^{24 (link)}.

Schiattarella G.G., Altamirano F., Tong D., French K.M., Villalobos E., Kim S.Y., Luo X., Jiang N., May H.I., Wang Z.V., Hill T.M., Mammen P.P., Huang J., Lee D.I., Hahn V., Sharma K., Kass D.A., Lavandero S., Gillette T.G, & Hill J.A. (2019). Nitrosative Stress Drives Heart Failure with Preserved Ejection Fraction. Nature, 568(7752), 351-356.

Publication 2019

Adult Animals Animals, Laboratory Aortic Valve Stenosis arginine methyl ester Body Weight Caimans Diet Food Institutional Animal Care and Use Committees Lysine Males Mice, House Mice, Inbred C57BL Mice, Knockout Myocytes, Cardiac Myosin Heavy Chains NG-Nitroarginine Methyl Ester Nitric Oxide Synthase Type II NOS2A protein, human Obesity Operative Surgical Procedures Rats, Inbred WKY Rattus norvegicus Rivers Strains Tetracycline Trans-Activators Transcription Factor

Most recents protocols related to «Myosin Heavy Chains»

Quantifying Cardiac Gene Expression in H9c2 Cells

Total RNA was extracted from H9c2 cells using the MAXWELL^®16 LEV simply RNA tissue Kit (Promega, Madison, WI) and the MAXWELL^® 16 instrument (Promega) in accordance with the manufacturer’s instructions. Complementary DNA was synthesized from 1 μg of total RNA with the PrimeScript RT Reagent Kit (Takara Bio Inc., Shiga, Japan). Real-time polymerase chain reaction (PCR) was performed using SYBR Premix Ex Taq™ (Takara Bio Inc.) and the Applied Biosystems 7,500 Real Time PCR System (Applied Biosystems, Foster, CA). Rat Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was amplified as an internal control. Expression analysis was performed by the Delta-Delta Ct method using 7500 Software v2.3 (Applied Biosystems). The primers used for these experiments were as follows: rat atrial natriuretic factor (ANF), forward 5′-ATGGGCTCCTTCTCCATCAC-3′ and reverse 5′-TTCATCGGTATGCTCGCTCA-3′; rat brain natriuretic peptide (BNP), forward 5′-TGGGAAGTCCTAGCCAGTCT-3′ and reverse 5′-GATCCGGTCTATCTTCTGCC-3′; rat β-myosin heavy chain (beta MHC), forward 5′-CTAGGAGGCGGAGGAACAG-3′ and reverse 5′-CTTGGCGCCAATGTCACG-3′; rat alpha smooth muscle actin (alpha SMA), forward 5′-GACACCAGGGAGTGATGGTT-3′ and reverse 5′-GTTAGCAAGGTCCGATGCTC-3′; rat collagen I, forward 5′-TGCCGTGACCTCAAGATGTG-3′ and reverse 5′-CACAAGCGTGCTGTAGGTGA-3′; rat FGF23, forward 5′-GCAACATTTTTGGATCGTATCA-3′ and reverse 5′-GATGCTT CGGTGACAGGTAGA-3′; rat N-acetylgalactosaminyltransferase 3 (GALNT3), forward 5′-GTTGCTAGGAGCAACAGTCGCA-3′ and reverse 5′-AGTTCACCGTGGTAGTATTGTAGT-3′; and rat GAPDH, forward 5′-GGCACAGTCAAGGCTGAGAATG-3′ and reverse 5′-ATGGTGGTGAAGACGCCAGTA-3′.

Kishimoto H., Nakano T., Torisu K., Tokumoto M., Uchida Y., Yamada S., Taniguchi M, & Kitazono T. (2023). Indoxyl sulfate induces left ventricular hypertrophy via the AhR-FGF23-FGFR4 signaling pathway. Frontiers in Cardiovascular Medicine, 10, 990422.

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Publication 2023

ACTA2 protein, human atrial natriuretic peptide, rat Collagen Type I DNA, Complementary FGF23 protein, human Glyceraldehyde-3-Phosphate Dehydrogenases Myosin Heavy Chains natriuretic peptide precursor type B, rat Oligonucleotide Primers Promega Real-Time Polymerase Chain Reaction smooth muscle actin, rat Tissues

Inducible Cardiac-Specific Cavβ2a Overexpression

FVB mouse strain was used in our study. Cardiac myocyte specific [α-myosin heavy chain (MHC) promoter] with inducible tetracycline-activator (tTA) expression of the β2a-subunit of L-type Ca²⁺ channel (Cavβ2a) was used. This β2a-Tg with relatively low expression level was documented (Supplemental Fig. S3; all Supplemental material is available at https://www.doi.org/10.6084/m9.figshare.22068815) (21 (link)). The overexpression of β2a-subunit increases the open probability and membrane trafficking of the pore-forming Cav1.2α1c-subunit, which further increased Ca²⁺ influx in cardiomyocytes as previously reported (21 (link), 22 (link)).
The β2a-Tg mice were established with the inducible (tet-off), bitransgenic system (22 (link)) (Supplemental Fig. S3). Mice with the tetracycline transactivator (tTA) driver gene and the Cavβ2a gene (double transgenic, DTG) without the doxycycline-containing chow were used as our β2a-Tg experimental group. Doxycycline is a derivative of tetracycline and hence represses β2a transgene expression. The Cavβ2a transgene was not expressed until adulthood to avoid developmental complications (22 (link)). For each litter, β2a-Tg mice were separated into different treatment cohorts, and their WT mice littermates were separated into corresponding treatments as well. Sex-matched animals (β2a-Tg and WT mice) were given different treatments at the age of 4 mo when the Cavβ2a gene had been fully expressed.

Li Y., Kubo H., Yu D., Yang Y., Johnson J.P., Eaton D.M., Berretta R.M., Foster M., McKinsey T.A., Yu J., Elrod J.W., Chen X, & Houser S.R. (2023). Combining three independent pathological stressors induces a heart failure with preserved ejection fraction phenotype. American Journal of Physiology - Heart and Circulatory Physiology, 324(4), H443-H460.

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Publication 2023

Animals Animals, Transgenic CAV1 protein, human Doxycycline Genes Mice, Laboratory Myocytes, Cardiac Myosin Heavy Chains Protein Subunits Strains Tetracycline Tissue, Membrane Trans-Activators Transgenes

Myosin Heavy Chain Isoform Identification

The antibodies for three myosin heavy chain (MyHC) isoforms (MyHC1, MyHC2A, and MyHC2X) and laminin were used as described by Riaz et al., 2016 (link). Briefly, cryosections were stained with rabbit anti‐laminin (1:1000, Sigma-Aldrich, L9393) and mouse anti‐6H1 (1:5, DSHB; AB_2314830) detecting MyHC2X, for two hours at room temperature. Following the PBST washing, the secondary antibodies goat anti‐rabbit‐conjugated‐Alexa Fluor 750 (1:1000, Thermo Fisher Scientific, A21039) and goat anti‐mouse‐conjugated‐Alexa Fluor 488 (1:1000, A11001, Thermo Fisher Scientific) were incubated for an hour at room temperature. After PBST washing, sections were incubated overnight at four degrees with a mix of fluorescently conjugated monoclonal antibodies: BA‐D5‐conjugated‐Alexa Fluor 350 (1:600, DSHB, AB_2235587) and SC‐71‐conjugated‐Alexa Fluor 594 (1:700, DSHB, AB_2147165), detecting MyHC1 and MyHC2A, respectively. Lastly, after washing with PBST, the cryosections were mounted with ProLong Gold antifade reagent (P36930, Thermo Fisher Scientific) and stored at four degrees prior to imaging.

Abbassi-Daloii T., el Abdellaoui S., Voortman L.M., Veeger T.T., Cats D., Mei H., Meuffels D.E., van Arkel E., 't Hoen P.A., Kan H.E, & Raz V. (2023). A transcriptome atlas of leg muscles from healthy human volunteers reveals molecular and cellular signatures associated with muscle location. eLife, 12, e80500.

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Publication 2023

Alexa 350 Alexa594 alexa fluor 488 Alexa Fluor 750 Antibodies Cryoultramicrotomy Goat Gold Laminin Mice, House Monoclonal Antibodies Myosin Heavy Chains Protein Isoforms Rabbits

Smooth Muscle Cell-Specific BDNF Knockout

All animal experiments were approved by the local authorities of Regierungspräsidium Giessen (GI 20/10, number 92/2010 and 24/2015 for hypoxic experiments; GI 20/10 number 63/2012 for PAB; GI 20/10 number 115/2014 for cell isolation) and in compliance with the guidelines from directive 2010/63/EU of the European Parliament on the protection of animals used for scientific purposes and to the Declaration of Helsinki. All mice used in this study were adult males with a weight of 20–30 g. For the hypoxic experiments, Smmhc-CreERT2 mice (Tg(Myh11-cre/ERT2)) mice were obtained from Stefan Offermanns (Max Planck Institute for Heart and Lung Research, Bad Nauheim, Germany) and crossbred with BDNF-floxed mice (Bdnf^tm3Jae/J) from the Jackson Laboratory to obtain mice expressing tamoxifen-inducible Cre-recombinase under the promoter of smooth muscle myosin heavy chain (Myh11, also known as Smmhc) and Bdnf flanked by loxP sites (Bdnf/Smmhc). Induction of the smooth muscle cell (SMC)-type specific knockout was achieved by tamoxifen feeding 10 days prior to normoxic or hypoxic exposure. In total, three different groups were evaluated: the Bdnf/Smmhc control group without induction of the BDNF knockout by feeding with tamoxifen-free food; the Bdnf/Smmhc knockout group with induction of Bdnf knockout in SMCs by feeding with tamoxifen-containing food; and to evaluate the effect of tamoxifen feeding, we additionally analysed Cre-negative, Bdnf-floxed mice that were fed with tamoxifen without induction of BDNF knockout (Smmhc control group).
For the PAB experiments, mice heterozygous for the Bdnftm1Jae mutation (B6.129S4-Bdnftm^1Jae^/J, Bdnf⁺^/−), which show approximately half normal levels of Bdnf mRNA, originating from the Jackson Laboratory and bred in our local animal facility, were used. For the control, we used littermates without mutation (WT) bred in our local animal facility. For cell isolation, WT (C57BL/6J) mice were obtained from the Jackson Laboratory. Numbers given for in vivo measurements may vary for different parameters due to technical issues (e.g. displacement of catheter).

Schäfer K., Tello K., Pak O., Richter M., Gierhardt M., Kwapiszewska G., Veith C., Fink L., Gall H., Hecker M., Kojonazarov B., Kraut S., Lo K., Wilhelm J., Grimminger F., Seeger W., Schermuly R.T., Ghofrani H.A., Zahner D., Gerstberger R., Weissmann N., Sydykov A, & Sommer N. (2023). Decreased plasma levels of the brain-derived neurotrophic factor correlate with right heart congestion in pulmonary arterial hypertension. ERJ Open Research, 9(2), 00230-2022.

Publication 2023

Adult Animals Catheters Cell Separation Cre recombinase Europeans Food Heart Heterozygote Hypoxia Lung Males Mice, Inbred C57BL mitogen-activated protein kinase 3, human Mus Mutation MYH11 protein, human Myocytes, Smooth Muscle Myosin Heavy Chains RNA, Messenger Smooth Muscles Tamoxifen

Cardiac Gene Expression Analysis

Samples from the LV were separated, flash frozen in liquid nitrogen, and stored at −80°C until RNA isolation was completed. Total RNA was extracted using the Eastep Super Total RNA Extraction Kit (LS1040, Promega) and reverse transcribed with HiScript III RT SuperMix (R323-01, Vazyme). Quantitative real-time PCR was conducted using the ChamQ Universal SYBR qPCR Master Mix (Q711-02, Vazyme). The primers were as follows: Brain natriuretic peptide (BNP), forward 5′-GAGGTCACTCCTATCCTCTGG-3, reverse 5′-GCCATTTCCTCCGACTTTTCTC-3’; β-myosin heavy chain (βMHC), forward 5′-ACTGTCAACACTAAGAGGGTCA-3, reverse 5′-TTGGATGATTTGATCTTCCAGGG-3’; and Glyceraldehyde-phosphate dehydrogenase (GAPDH): forward 5′-GCAAATTCAACGGCACAGTCAAGG-3′, reverse 5′-TCTCGTGGTTCACACCCATCACAA-3′, and all primers in this study were purchased from Sangon Biotech Co., Ltd (Shanghai). The target gene expression was calculated using the 2^−ΔΔCT method, and the GAPDH gene level was used to normalize the expression of the target gene.

Wang Z., Zhao X., Bu L., Liu K., Li Z., Zhang H., Zhang X., Yuan F., Wang S., Guo Z, & Shi L. (2023). Low sodium intake ameliorates hypertension and left ventricular hypertrophy in mice with primary aldosteronism. Frontiers in Physiology, 14, 1136574.

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Publication 2023

Freezing Gene Expression Genes Glyceraldehyde-3-Phosphate Dehydrogenases isolation Myosin Heavy Chains Nesiritide Nitrogen Oligonucleotide Primers Promega Real-Time Polymerase Chain Reaction

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What are the different types or isoforms of Myosin Heavy Chains?

Myosin Heavy Chains exhibit a diverse range of isoforms that are expressed in various muscle types and tissues. Some of the major isoforms include slow/beta, fast/alpha, and cardiac-specific Myosin Heavy Chains. These isoforms have distinct structural and functional properties that contribute to the specialized roles of different muscle types, such as slow-twitch, fast-twitch, and cardiac muscle.

How do Myosin Heavy Chains generate force and motion within cells?

Myosin Heavy Chains are the 'heavy' portion of the myosin protein complex, which plays a critical role in the generation of force and cellular movement. These large polypeptide chains interact with actin filaments, and through a cyclic process of ATP hydrolysis and conformational changes, they can produce the necessary force to drive muscle contraction and other cellular movements.

What are some common applications of Myosin Heavy Chains in research?

Myosin Heavy Chains are widely studied in various fields of research, including muscle physiology, cell biology, and biomechanics. Researchers may investigate the role of Myosin Heavy Chains in muscle development, disease pathologies, and cellular processes such as cytokinesis and organelle transport. Additionally, Myosin Heavy Chains can be used as biomarkers for certain muscle-related conditions and as targets for therapeutic interventions.

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More about "Myosin Heavy Chains"

Myosin Heavy Chains (MHCs) are a class of motor proteins that play a crucial role in muscle contraction and cellular movement.
These large polypeptide chains form the 'heavy' portion of the myosin protein complex, generating the force and motion necessary for various cellular processes.
MHCs exhibit diverse isoforms and tissue distributions, contributing to the specialized functions of different muscle types, including skeletal, cardiac, and smooth muscle.
Researchers investigating MHCs can leverage the power of PubCompare.ai's AI-driven platform to optimize their research protocols.
The platform helps users locate the best published methods from literature, pre-prints, and patents, ensuring reproducibility and accuracy through AI-driven comparisons.
This can be particularly helpful when working with related techniques and reagents, such as Alexa Fluor 488 (a fluorescent dye used for labeling proteins), DAPI (a nuclear stain), TRIzol reagent (a solution for RNA extraction), Triton X-100 (a detergent used for cell lysis), Bovine serum albumin (a common protein used in cellular assays), SC-71 (a myosin heavy chain antibody), and FBS (fetal bovine serum, a cell culture supplement).
By utilizing PubCompare.ai's AI-driven platform, researchers can unlock new insights and advance their MHCs research to new heights, ensuring their protocols are optimized for reproducibility, accuracy, and efficiency.
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